RPOB_MYCLE
ID RPOB_MYCLE Reviewed; 1178 AA.
AC P30760;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=ML1891;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8446028; DOI=10.1111/j.1365-2958.1993.tb01112.x;
RA Honore N.T., Bergh S., Chanteau S., Doucet-Populaire F., Eiglmeier K.,
RA Garnier T., Georges C., Launois P., Limpaiboon T., Newton S., Niang K.,
RA del Portillo P., Ramesh G.R., Reddi P., Ridel P.R., Sittisombut N.,
RA Wu-Hunter S., Cole S.T.;
RT "Nucleotide sequence of the first cosmid from the Mycobacterium leprae
RT genome project: structure and function of the Rif-Str regions.";
RL Mol. Microbiol. 7:207-214(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01321};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z14314; CAA78668.1; -; Genomic_DNA.
DR EMBL; AL583923; CAC30845.1; -; Genomic_DNA.
DR PIR; E87145; E87145.
DR PIR; S31145; S31145.
DR RefSeq; NP_302273.1; NC_002677.1.
DR AlphaFoldDB; P30760; -.
DR SMR; P30760; -.
DR STRING; 272631.ML1891; -.
DR EnsemblBacteria; CAC30845; CAC30845; CAC30845.
DR KEGG; mle:ML1891; -.
DR PATRIC; fig|272631.5.peg.3581; -.
DR Leproma; ML1891; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_11; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.30.150.10; -; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR02013; rpoB; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1178
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047920"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 554..560
FT /note="FLEPRVL -> SSSRACW (in Ref. 1; CAA78668)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="A -> R (in Ref. 1; CAA78668)"
FT /evidence="ECO:0000305"
FT CONFLICT 724..731
FT /note="MPWEGHNY -> NAVGGSTTN (in Ref. 1; CAA78668)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1178 AA; 129728 MW; C8720D1A44C556FA CRC64;
MLEGCILPDF GQSKTDVSPS QSRPQSSPNN SVPGAPNRIS FAKLREPLEV PGLLDVQTDS
FEWLIGSPCW RAAAASRGDL KPVGGLEEVL YELSPIEDFS GSMSLSFSDP RFDEVKAPVE
ECKDKDMTYA APLFVTAEFI NNNTGEIKSQ TVFMGDFPMM TEKGTFIING TERVVVSQLV
RSPGVYFDET IDKSTEKTLH SVKVIPSRGA WLEFDVDKRD TVGVRIDRKR RQPVTVLLKA
LGWTSEQITE RFGFSEIMRS TLEKDNTVGT DEALLDIYRK LRPGEPPTKE SAQTLLENLF
FKEKRYDLAR VGRYKVNKKL GLHAGELITS STLTEEDVVA TIEYLVRLHE GQSTMTVPGG
VEVPVETDDI DHFGNRRLRT VGELIQNQIR VGMSRMERVV RERMTTQDVE AITPQTLINI
RPVVAAIKEF FGTSQLSQFM DQNNPLSGLT HKRRLSALGP GGLSRERAGL EVRDVHPSHY
GRMCPIETPE GPNIGLIGSL SVYARVNPFG FIETPYRKVV DGVVSDEIEY LTADEEDRHV
VAQANSPIDE AGRFLEPRVL VRRKAGEVEY VASSEVDYMD VSPRQMVSVA TAMIPFLEHD
DANRALMGAN MQRQAVPLVR SEAPLVGTGM ELRAAIDAGH VVVAEKSGVI EEVSADYITV
MADDGTRRTY RMRKFARSNH GTCANQSPIV DAGDRVEAGQ VIADGPCTEN GEMALGKNLL
VAIMPWEGHN YEDAIILSNR LVEEDVLTSI HIEEHEIDAR DTKLGAEEIT RDIPNVSDEV
LADLDERGIV RIGAEVRDGD ILVGKVTPKG ETELTPEERL LRAIFGEKAR EVRDTSLKVP
HGESGKVIGI RVFSHEDDDE LPAGVNELVR VYVAQKRKIS DGDKLAGRHG NKGVIGKILP
AEDMPFLPDG TPVDIILNTH GVPRRMNVGQ ILETHLGWVA KSGWKIDVAG GIPDWAVNLP
EELLHAAPNQ IVSTPVFDGA KEEELQGLLS STLPNRDGDV MVGGDGKAVL FDGRSGEPFP
YPVTVGYMYI MKLHHLVDDK IHARSTGPYS MITQQPLGGK AQFGGQRFGE MECWAMQAYG
AAYTLQELLT IKSDDTVGRV KVYEAIVKGE NIPEPGIPES FKVLLKELQS LCLNVEVLSS
DGAAIELREG EDEDLERAAA NLGINLSRNE SASIEDLA
